title: Purification, properties and assembly of the neck-appendage protein of the Bacillus subtilis phage phi 29.
abstract: The purification of the neck appendage protein of phi 29, p12*, which is involved in the adsorption of the phage to Bacillus subtilis, is described. The purified native protein is in a dimeric form and can be assembled, in vitro, onto purified 12- particles that lack the neck appendages, suggesting that the incorporation of p12* to the rest of the phage structure is a self-assembly process. The assembly of protein p12* in vitro follows cooperative kinetics and it occurs with an efficiency of about 4%.
mesh_terms: D001412:Bacillus subtilis / Q000378:metabolism*; D001435:Bacteriophages / Q000378:metabolism*; D005816:Genetic Complementation Test; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D014764:Viral Proteins / Q000096:biosynthesis / Q000302:isolation & purification*
chemical_list: D014764:Viral Proteins